Evidence map›Paper›PMID 9463366›Full record

ArticleThe EMBO journal1998

The first step of glycosylphosphatidylinositol biosynthesis is mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1.

R Watanabe, N Inoue, B Westfall, C H Taron, P Orlean, J Takeda, T Kinoshita

Abstract read
In one paragraph

Article in The EMBO journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed, 1 pooled it
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

78 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. PIGC-related encephalopathy: Lessons learned from 18 new probands.European journal of human genetics : EJHG · 2025
    Article
  9. Article
  10. Review
  11. Article
  12. X-Linked Epilepsies: A Narrative Review.International journal of molecular sciences · 2024
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

18 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

R WatanabeDepartment of Immunoregulation, Research Institute for Microbial Diseases, Osaka University, Japan.
N Inoue
B Westfall
C H Taron
P Orlean
J Takeda
T Kinoshita

Funding

PATHWAYS FOR GLYCOSYLPHOSPHATIDYLINOSITOL ASSEMBLYR01GM046220 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI ORLEAN, PETER AB · 1991 to 2003
$1.1M
NIGMS NIH HHS GM46220
6 · The paper itself

Abstract

Biosynthesis of glycosylphosphatidylinositol (GPI) is initiated by transfer of N-acetylglucosamine (GlcNAc) from UDP-GlcNAc to phosphatidylinositol (PI). This chemically simple step is genetically complex because three genes are required in both mammals and yeast. Mammalian PIG-A and PIG-C are homologous to yeast GPI3 and GPI2, respectively; however, mammalian PIG-H is not homologous to yeast GPI1. Here, we report cloning of a human homolog of GPI1 (hGPI1) and demonstrate that four mammalian gene products form a protein complex in the endoplasmic reticulum membrane. PIG-L, which is involved in the second step in GPI synthesis, GlcNAc-PI de-N-acetylation, did not associate with the isolated complex. The protein complex had GPI-GlcNAc transferase (GPI-GnT) activity in vitro, but did not mediate the second reaction. Bovine PI was utilized approximately 100-fold more efficiently than soybean PI as a substrate, and lyso PI was a very inefficient substrate. These results suggest that GPI-GnT recognizes the fatty acyl chains of PI. The unusually complex organization of GPI-GnT may be relevant to selective usage of PI and/or regulation.

Indexed as

Saccharomyces cerevisiae ProteinsAmino Acid SequenceBase SequenceCeramidesCloning, MolecularDNA, ComplementaryEnzyme ActivationGlutathione TransferaseGlycosylphosphatidylinositolsHexosyltransferasesHumansMacromolecular SubstancesMembrane ProteinsMolecular Sequence DataPhospholipidsSequence Homology, Amino AcidCeramidesDNA, ComplementaryGlutathione TransferaseGlycosylphosphatidylinositolsGPI1 protein, S cerevisiaeHexosyltransferasesMacromolecular SubstancesMembrane Proteinsphosphatidylinositol glycan-class A proteinPhospholipidsPIGC protein, humanPIGQ protein, humanSaccharomyces cerevisiae Proteins

Identifiers

PMID9463366
PMCPMC1170437

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.